Difference between revisions of "TrpE"
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− | * '''Description:''' anthranilate synthase <br/><br/> | + | * '''Description:''' anthranilate synthase (subunit I) <br/><br/> |
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|style="background:#ABCDEF;" align="center"| '''Essential''' || no | |style="background:#ABCDEF;" align="center"| '''Essential''' || no | ||
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− | |style="background:#ABCDEF;" align="center"| '''Product''' || anthranilate synthase | + | |style="background:#ABCDEF;" align="center"| '''Product''' || anthranilate synthase (subunit I) |
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|style="background:#ABCDEF;" align="center"|'''Function''' || biosynthesis of tryptophan | |style="background:#ABCDEF;" align="center"|'''Function''' || biosynthesis of tryptophan | ||
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* '''Effectors of protein activity:''' subject to feedback inhibition by tryptophan [http://www.ncbi.nlm.nih.gov/sites/entrez/19258532 PubMed] | * '''Effectors of protein activity:''' subject to feedback inhibition by tryptophan [http://www.ncbi.nlm.nih.gov/sites/entrez/19258532 PubMed] | ||
− | * '''Interactions:''' | + | * '''Interactions:''' [[PabA]]-[[TrpE]] |
* '''Localization:''' | * '''Localization:''' |
Revision as of 07:50, 11 June 2009
- Description: anthranilate synthase (subunit I)
Gene name | trpE |
Synonyms | |
Essential | no |
Product | anthranilate synthase (subunit I) |
Function | biosynthesis of tryptophan |
MW, pI | 57 kDa, 5.246 |
Gene length, protein length | 1545 bp, 515 aa |
Immediate neighbours | trpD, aroH |
Get the DNA and protein sequences (Barbe et al., 2009) | |
Genetic context This image was kindly provided by SubtiList
|
Contents
The gene
Basic information
- Locus tag: BSU22680
Phenotypes of a mutant
Database entries
- DBTBS entry: [1]
- SubtiList entry: [2]
Additional information
The protein
Basic information/ Evolution
- Catalyzed reaction/ biological activity: Chorismate + L-glutamine = anthranilate + pyruvate + L-glutamate (according to Swiss-Prot)
- Protein family:
- Paralogous protein(s):
Extended information on the protein
- Kinetic information:
- Domains:
- Modification:
- Cofactor(s):
- Effectors of protein activity: subject to feedback inhibition by tryptophan PubMed
- Localization:
Database entries
- Structure:
- Swiss prot entry: P03963
- KEGG entry: [3]
- E.C. number: 4.1.3.27
Additional information
Expression and regulation
- Regulatory mechanism: TRAP: binding to the mRNA in the presence of tryptophan, this results in transcription termination PubMed
- Additional information: subject to feedback inhibition by tryptophan PubMed
Biological materials
- Mutant:
- Expression vector:
- lacZ fusion:
- GFP fusion:
- two-hybrid system:
- Antibody:
Labs working on this gene/protein
Your additional remarks
References
Paul Gollnick, Paul Babitzke, Alfred Antson, Charles Yanofsky
Complexity in regulation of tryptophan biosynthesis in Bacillus subtilis.
Annu Rev Genet: 2005, 39;47-68
[PubMed:16285852]
[WorldCat.org]
[DOI]
(P p)
Gintaras Deikus, Paul Babitzke, David H Bechhofer
Recycling of a regulatory protein by degradation of the RNA to which it binds.
Proc Natl Acad Sci U S A: 2004, 101(9);2747-51
[PubMed:14976255]
[WorldCat.org]
[DOI]
(P p)
J Otridge, P Gollnick
MtrB from Bacillus subtilis binds specifically to trp leader RNA in a tryptophan-dependent manner.
Proc Natl Acad Sci U S A: 1993, 90(1);128-32
[PubMed:8419914]
[WorldCat.org]
[DOI]
(P p)
P Babitzke, P Gollnick, C Yanofsky
The mtrAB operon of Bacillus subtilis encodes GTP cyclohydrolase I (MtrA), an enzyme involved in folic acid biosynthesis, and MtrB, a regulator of tryptophan biosynthesis.
J Bacteriol: 1992, 174(7);2059-64
[PubMed:1551827]
[WorldCat.org]
[DOI]
(P p)
H Shimotsu, M I Kuroda, C Yanofsky, D J Henner
Novel form of transcription attenuation regulates expression the Bacillus subtilis tryptophan operon.
J Bacteriol: 1986, 166(2);461-71
[PubMed:2422155]
[WorldCat.org]
[DOI]
(P p)
D J Henner, L Band, H Shimotsu
Nucleotide sequence of the Bacillus subtilis tryptophan operon.
Gene: 1985, 34(2-3);169-77
[PubMed:3924737]
[WorldCat.org]
[DOI]
(P p)
H Shimotsu, D J Henner
Characterization of the Bacillus subtilis tryptophan promoter region.
Proc Natl Acad Sci U S A: 1984, 81(20);6315-9
[PubMed:6436812]
[WorldCat.org]
[DOI]
(P p)
- Author1, Author2 & Author3 (year) Title Journal volume: page-page. PubMed